EGLN1/PHD2 Recombinant Protein Antigen
Novus Biologicals, part of Bio-Techne | Catalog # NBP2-54676PEP
Key Product Details
Source
E. coli
Conjugate
Unconjugated
Applications
Antibody Competition
Product Specifications
Description
A recombinant protein antigen with a N-terminal His6-ABP tag corresponding to human EGLN1/PHD2.
Source: E. coli
Amino Acid Sequence: GICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKING
Fusion Tag: N-terminal His6ABP (ABP = Albumin Binding Protein derived from Streptococcal Protein G)
This product is intended to be used as a blocking antigen for antibody competition assays. Any other use of this antigen is done at the risk of the user. The use of this product for commercial production is strictly prohibited. Please contact technical support if you have any questions.
Purity
>80% by SDS-PAGE and Coomassie blue staining
Predicted Molecular Mass
27 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Applications
Antibody Competition (10 - 100 molar excess)
Application Notes
This recombinant antigen is only intended to be used as a blocking agent to confirm antibody specificity with the corresponding antibody, catalog number NBP2-54676.
It is purified by IMAC chromatography, and the expected concentration is greater than 0.5 mg/ml.
For current lot information, including availability, please contact our technical support team click nb-technical@bio-techne.com
For further blocking tide related information and a protocol, click here.
Protein / Peptide Type
Recombinant Protein Antigen
Formulation, Preparation and Storage
NBP2-54676PEP
| Formulation | PBS, 1 M Urea (pH 7.4) |
| Preservative | No Preservative |
| Concentration | Please see the vial label for concentration. If unlisted please contact technical services. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage | Store at -20C. Avoid freeze-thaw cycles. |
Background: EGLN1/PHD2
EGLN1/PHD2 has been implicated in several critical processes including erythropoiesis, angiogenesis, and metabolism as well as various pathologies such as cancer (2, 5, 6). Studies in mice have found that somatic deletion of PHD2 resulted in higher vascular endothelial growth factor A (VEGF-A) levels, increased blood vessel formation, and more erythropoietin (EPO), leading to severe polycythemia or erythrocytosis (high red blood cell (RBC) volume) (6). Another study revealed that specific point mutations in EGLN1/PHD2 led to elevated EPO and RBC mass associated with hemorrhages and strokes (6). Accordingly, given the known role of PHD2 in inhibition of EPO production, PHD2 inhibitors are being studied as a potential therapeutic for anemia (6). Additionally, dysregulation in EGLN1, and specifically the PHD2-VHL-HIF-1alpha pathway, has been associated with the development of pheochromocytomas (PCC) and sympathetic paragangliomas (PGL), which are rare neuroendocrine tumors (2). Besides pathological features, EGLN1/PHD2 may also be important for high altitude adaptation as two coding sequence variants in PHD2 are prevalent in the Tibetan population but is very rare in people at lower altitudes (2).
Alternate names for EGLN1/PHD2 include HIF Prolyl Hydroxylase 2, PH2, Prolyl hydroxylase domain containing protein 2, HIF2PH2, HIF-Prolyl hydroxylase 2, egl nine homolog 1, and C1orf12.
References
1. Amorim-Pires, D., Peixoto, J., & Lima, J. (2016). Hypoxia Pathway Mutations in Pheochromocytomas and Paragangliomas. Cytogenetic and genome research. https://doi.org/10.1159/000457479
2. Gardie, B., Percy, M. J., Hoogewijs, D., Chowdhury, R., Bento, C., Arsenault, P. R., Richard, S., Almeida, H., Ewing, J., Lambert, F., McMullin, M. F., Schofield, C. J., & Lee, F. S. (2014). The role of PHD2 mutations in the pathogenesis of erythrocytosis. Hypoxia (Auckland, N.Z.). https://doi.org/10.2147/HP.S54455
3. Minervini, G., Quaglia, F., & Tosatto, S. C. (2015). Insights into the proline hydroxylase (PHD) family, molecular evolution and its impact on human health. Biochimie. https://doi.org/10.1016/j.biochi.2015.07.009
4. Semenza G. L. (2007). Hypoxia-inducible factor 1 (HIF-1) pathway. Science's STKE : signal transduction knowledge environment. https://doi.org/10.1126/stke.4072007cm8
5. Chan, D. A., & Giaccia, A. J. (2010). PHD2 in tumour angiogenesis. British journal of cancer. https://doi.org/10.1038/sj.bjc.6605682
6. Meneses, A. M., & Wielockx, B. (2016). PHD2: from hypoxia regulation to disease progression. Hypoxia (Auckland, N.Z.). https://doi.org/10.2147/HP.S53576
Long Name
Egl Nine Homolog 1/Prolyl Hydroxylase Domain-containing Protein 2
Alternate Names
C1orf12, HIFPH2, HPH2, PHD2, SM20, ZMYND6
Gene Symbol
EGLN1
Additional EGLN1/PHD2 Products
Product Documents for EGLN1/PHD2 Recombinant Protein Antigen
Product Specific Notices for EGLN1/PHD2 Recombinant Protein Antigen
This product is for research use only and is not approved for use in humans or in clinical diagnosis. This product is guaranteed for 1 year from date of receipt.
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